1e08

Structural model of the [Fe]-hydrogenase/cytochrome C553 complex combining NMR and soft-docking
The complex shows the specific interaction of the hydrogenase (light blue) with the cytochrome (pink), revealing the path of electron transport from the active site metal cluster, through three iron-sulfur clusters, and ending in the cytochrome heme (colored red). Two cysteine amino acids at the interface, CYS 38 in the hydrogenase and CYS10 in the cytochrome, are thought to provide the electron transfer pathway between the two proteins.

This section complements the article on Hydrogenase in the Molecule of the Month Series. See also Teaching Scenes, Tutorials, and Educators' Pages.

About this Structure
1E08 is a Protein complex structure of Fe-hydrogenase from Desulfovibrio desulfuricans and one of its electron transfer partners, cytochrome c553, taken from the related organism Desulfovibrio vulgaris. Full experimental information is available from OCA.

Reference
Structural model of the Fe-hydrogenase/cytochrome c553 complex combining transverse relaxation-optimized spectroscopy experiments and soft docking calculations., Morelli X, Czjzek M, Hatchikian CE, Bornet O, Fontecilla-Camps JC, Palma NP, Moura JJ, Guerlesquin F, J Biol Chem. 2000 Jul 28;275(30):23204-10. PMID:10748163

Page seeded by OCA on Mon Jun 30 23:55:28 2008